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Crystal structure of fumarate hydratase class II from elizabethkingia anophelis NUHP1
Analyse Crystal structure of fumarate hydratase class II from elizabethkingia anophelis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MIW
- Type
- protein
- Length
- 1,854 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fumarate hydratase class II
- EC
- 4.2.1.2
- UniProt
- A0A077EJP9
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fumarate hydratase class II (EC 4.2.1.2) | protein | 463 | 61% helix, 8% strand | A0A077EJP9 |
| C, D | Fumarate hydratase class II (EC 4.2.1.2) | protein | 464 | 61% helix, 8% strand | A0A077EJP9 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.77 | 0.98 | 24 | empty |
| 2 | 811 | 0.76 | 0.81 | 71 | empty |
| 3 | 924 | 0.75 | 0.79 | 70 | empty |
| 4 | 56 | 0.73 | 0.99 | 16 | EDO |
| 5 | 55 | 0.68 | 0.97 | 16 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3488 Ų buried · 30 hydrogen bonds · protein-protein
- A–B · 3037 Ų buried · 26 hydrogen bonds · protein-protein
- A–D · 2540 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 2540 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 2079 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 7MIW · Crystal Structure of Fumarate hydratase class II from Elizabethkingia anophelis NUHP1 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A077EJP9
- Elsewhere: RCSB PDB 7MIW · PDBe 7MIW · UniProt A0A077EJP9
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